3ap2: Difference between revisions

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<StructureSection load='3ap2' size='340' side='right'caption='[[3ap2]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
<StructureSection load='3ap2' size='340' side='right'caption='[[3ap2]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3ap2]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AP2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3AP2 FirstGlance]. <br>
<table><tr><td colspan='2'>[[3ap2]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AP2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3AP2 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=A3P:ADENOSINE-3-5-DIPHOSPHATE'>A3P</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3ap1|3ap1]], [[3ap3|3ap3]]</div></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=A3P:ADENOSINE-3-5-DIPHOSPHATE'>A3P</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TPST2 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Protein-tyrosine_sulfotransferase Protein-tyrosine sulfotransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.8.2.20 2.8.2.20] </span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3ap2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ap2 OCA], [https://pdbe.org/3ap2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ap2 RCSB], [https://www.ebi.ac.uk/pdbsum/3ap2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ap2 ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3ap2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ap2 OCA], [https://pdbe.org/3ap2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ap2 RCSB], [https://www.ebi.ac.uk/pdbsum/3ap2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ap2 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/TPST2_HUMAN TPST2_HUMAN]] Catalyzes the O-sulfation of tyrosine residues within acidic motifs of polypeptides.  
[https://www.uniprot.org/uniprot/TPST2_HUMAN TPST2_HUMAN] Catalyzes the O-sulfation of tyrosine residues within acidic motifs of polypeptides.


==See Also==
==See Also==
*[[Sulfotransferase|Sulfotransferase]]
*[[Sulfotransferase 3D structures|Sulfotransferase 3D structures]]
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Protein-tyrosine sulfotransferase]]
[[Category: Adachi R]]
[[Category: Adachi, R]]
[[Category: Fujikawa Y]]
[[Category: Fujikawa, Y]]
[[Category: Kakuta Y]]
[[Category: Kakuta, Y]]
[[Category: Kawaguchi Y]]
[[Category: Kawaguchi, Y]]
[[Category: Kimura M]]
[[Category: Kimura, M]]
[[Category: Kurogi K]]
[[Category: Kurogi, K]]
[[Category: Liu M-C]]
[[Category: Liu, M C]]
[[Category: Mishiro-Sato E]]
[[Category: Mishiro-Sato, E]]
[[Category: Nakanishi Y]]
[[Category: Nakanishi, Y]]
[[Category: Sakakibara Y]]
[[Category: Sakakibara, Y]]
[[Category: Soejima M]]
[[Category: Soejima, M]]
[[Category: Suiko M]]
[[Category: Suiko, M]]
[[Category: Teramoto T]]
[[Category: Teramoto, T]]
[[Category: Sulfotransferase fold]]
[[Category: Transferase]]

Latest revision as of 18:50, 4 October 2023

Crystal structure of human tyrosylprotein sulfotransferase-2 complexed with PAP,C4 peptide, and phosphate ionCrystal structure of human tyrosylprotein sulfotransferase-2 complexed with PAP,C4 peptide, and phosphate ion

Structural highlights

3ap2 is a 4 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.4Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

TPST2_HUMAN Catalyzes the O-sulfation of tyrosine residues within acidic motifs of polypeptides.

See Also

3ap2, resolution 2.40Å

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OCA